Ser687
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Home > Phosphorylation Site Page: > Ser687  -  SCN2A (rat)

Site Information
EIRKRRsssyHVsMD   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 451194

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 3 , 4 ) , mass spectrometry ( 1 ) , mutation of modification site ( 2 , 3 ) , phosphopeptide mapping ( 4 )
Relevant cell line - cell type - tissue:
brain ( 1 ) , CHO (fibroblast) [EphB1 (human), transfection] ( 4 ) , oocyte [CPEB (mouse)] ( 3 ) , tsA201 (epithelial) ( 2 )

Upstream Regulation
Putative in vivo kinases:
PKACA (rat) ( 3 , 4 )
Kinases, in vitro:
PKACA (cow) ( 4 )
Phosphatases, in vitro:
PPP1CA (rat) ( 4 )
Treatments:
cAMP_analog ( 4 ) , colforsin ( 3 )

Downstream Regulation
Effects of modification on SCN2A:
activity, induced ( 2 )

References 

1

Baek JH, Rubinstein M, Scheuer T, Trimmer JS (2014) Reciprocal Changes in Phosphorylation and Methylation of Mammalian Brain Sodium Channels in Response to Seizures. J Biol Chem 289, 15363-15373
24737319   Curated Info

2

Cantrell AR, et al. (2002) Molecular mechanism of convergent regulation of brain Na(+) channels by protein kinase C and protein kinase A anchored to AKAP-15. Mol Cell Neurosci 21, 63-80
12359152   Curated Info

3

Smith RD, Goldin AL (1997) Phosphorylation at a single site in the rat brain sodium channel is necessary and sufficient for current reduction by protein kinase A. J Neurosci 17, 6086-93
9236220   Curated Info

4

Murphy BJ, Rossie S, De Jongh KS, Catterall WA (1993) Identification of the sites of selective phosphorylation and dephosphorylation of the rat brain Na+ channel alpha subunit by cAMP-dependent protein kinase and phosphoprotein phosphatases. J Biol Chem 268, 27355-62
8262976   Curated Info